Katepsin e
| Katepsin e | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.23.34 | ||||||||
| CAS broj | 110910-42-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Katepsin e (EC 3.4.23.34, proteinaza sporog kretanja, eritrocitna membranska aspartinska proteinaza, SMP, eritrocitna membranska aspartinska proteinaza, EMAP, nepepsinska proteinaza, katepsin D-slična kiselinska proteinaza, katepsinska E-slična kiselinska proteinaza, katepsinska D-tip proteinaza) je enzim.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Aktivnost slična katepsinu D, sa malo širom specifičnošću
Ovaj enzim je prisutan u stomaku želucu, slezini i eritrocitnim membranama.
Reference
- ↑ Lapresle, C., Puizdar, V., Porchon-Bertolotto, C., Joukoff, E. and Turk, V. (1986). „Structural differences between rabbit cathepsin E and cathepsin D”. Biol. Chem. Hoppe-Seyler 367: 523-526. PMID 3741628.
- ↑ Yonezawa, S., Fujii, K., Maejima, Y., Tamoto, K., Mori, Y. and Muto, N. (1988). „Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form”. Arch. Biochem. Biophys. 267: 176-183. PMID 3058036.
- ↑ Jupp, R.A., Richards, A.D., Kay, J., Dunn, B.M., Wyckoff, J.B., Samloff, I.M. and Yamamoto, K. (1988). „Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E”. Biochem. J. 254: 895-898. PMID 3058118.
- ↑ Azuma, T., Pals, G., Mohandas, T.K., Couvreur, J.M. and Taggart, R.T. (1989). „Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases”. J. Biol. Chem. 264: 16748-16753. PMID 2674141.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Cathepsin+E
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
